| First Author | Kunz TH | Year | 2007 |
| Journal | Biochim Biophys Acta | Volume | 1770 |
| Issue | 8 | Pages | 1145-50 |
| PubMed ID | 17493758 | Mgi Jnum | J:124792 |
| Mgi Id | MGI:3722542 | Doi | 10.1016/j.bbagen.2007.04.002 |
| Citation | Kunz TH, et al. (2007) Interaction of receptor-activity-modifying protein1 with tubulin. Biochim Biophys Acta 1770(8):1145-50 |
| abstractText | Receptor-activity-modifying protein (RAMP) 1 is an accessory protein of the G protein-coupled calcitonin receptor-like receptor (CLR). The CLR/RAMP1 heterodimer defines a receptor for the potent vasodilatory calcitonin gene-related peptide. A wider tissue distribution of RAMP1, as compared to that of the CLR, is consistent with additional biological functions. Here, glutathione S-transferase (GST) pull-down, coimmunoprecipitation and yeast two-hybrid experiments identified beta-tubulin as a novel RAMP1-interacting protein. GST pull-down experiments indicated interactions between the N- and C-terminal domains of RAMP1 and beta-tubulin. Yeast two-hybrid experiments confirmed the interaction between the N-terminal region of RAMP1 and beta-tubulin. Interestingly, alpha-tubulin was co-extracted with beta-tubulin in pull-down experiments and immunoprecipitation of RAMP1 coprecipitated alpha- and beta-tubulin. Confocal microscopy indicated colocalization of RAMP1 and tubulin predominantly in axon-like processes of neuronal differentiated human SH-SY5Y neuroblastoma cells. In conclusion, the findings point to biological roles of RAMP1 beyond its established interaction with G protein-coupled receptors. |
